ID Q65FS8_BACLD Unreviewed; 799 AA.
AC Q65FS8; Q62R85;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Alpha-1,4 glucan phosphorylase {ECO:0000256|RuleBase:RU000587};
DE EC=2.4.1.1 {ECO:0000256|RuleBase:RU000587};
GN Name=glgP {ECO:0000313|EMBL:AAU24725.1};
GN OrderedLocusNames=BL01415 {ECO:0000313|EMBL:AAU24725.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU24725.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU24725.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- FUNCTION: Allosteric enzyme that catalyzes the rate-limiting step in
CC glycogen catabolism, the phosphorolytic cleavage of glycogen to produce
CC glucose-1-phosphate, and plays a central role in maintaining cellular
CC and organismal glucose homeostasis. {ECO:0000256|RuleBase:RU000587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-
CC glucosyl](n-1) + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:41732,
CC Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9586, ChEBI:CHEBI:15444,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.1;
CC Evidence={ECO:0000256|RuleBase:RU000587};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU000587};
CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006047, ECO:0000256|RuleBase:RU000587}.
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DR EMBL; CP000002; AAU24725.1; -; Genomic_DNA.
DR RefSeq; WP_003184651.1; NC_006322.1.
DR AlphaFoldDB; Q65FS8; -.
DR STRING; 279010.BL01415; -.
DR CAZy; GT35; Glycosyltransferase Family 35.
DR GeneID; 66214799; -.
DR KEGG; bli:BL01415; -.
DR PATRIC; fig|279010.13.peg.3299; -.
DR eggNOG; COG0058; Bacteria.
DR HOGENOM; CLU_010198_1_1_9; -.
DR Proteomes; UP000000606; Chromosome.
DR Bgee; BL01415; Expressed in ovary.
DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro.
DR GO; GO:0102250; F:linear malto-oligosaccharide phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0102499; F:SHG alpha-glucan phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd04300; GT35_Glycogen_Phosphorylase; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR InterPro; IPR011833; Glycg_phsphrylas.
DR InterPro; IPR000811; Glyco_trans_35.
DR NCBIfam; TIGR02093; P_ylase; 1.
DR PANTHER; PTHR11468; GLYCOGEN PHOSPHORYLASE; 1.
DR PANTHER; PTHR11468:SF3; GLYCOGEN PHOSPHORYLASE; 1.
DR Pfam; PF00343; Phosphorylase; 1.
DR PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU000587};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU000587};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000460-1,
KW ECO:0000256|RuleBase:RU000587};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606};
KW Transferase {ECO:0000256|RuleBase:RU000587, ECO:0000313|EMBL:AAU24725.1}.
FT MOD_RES 646
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000460-1"
SQ SEQUENCE 799 AA; 92122 MW; 46C93C465F64A2D6 CRC64;
MFSSKESFKQ CFLKRVERLC GKSFRDSSTL DQYQTLGIMV REHISANWIE TNERSRSNQN
KQTYYLSIEF LLGRLLGQNL LNLGVREIVK EGLTELGICL EDIEEAEMDA GLGNGGLGRL
AACFLDSLAS LDLPGHGMGI RYKHGFFEQK IVDGHQVELP EQWLKHGYVW EIRNADQAVC
VRFGGRVKMA QEGGRLRFWQ EDAEVMTAVP HDIPIIGYET KTVNTLRLWN AEPCSLHHEP
NILKYKRETE AVSECLYPDD THDEGKILRL KQQYFLVSAS LQSIVKRYKN THPSLHDFHQ
KVAIHINDTH PALAVPELMR ILLDEEKMTW DEAWHVTVHT ISYTNHTTLA EALEKWRIDL
IKPLLPRIYM IIEEINERFC GWLWEKYPGE WERIEKLAVI AHGEVKMAHL AIVGSYSVNG
VANIHSTILK EREMNDFYSV FPFKFNNKTN GISHRRWLLK ANPPLANLIT EAIGDRWLKD
PESLLDLRPF ANDSAFLESF QRIKRERKQL LADMMKGSVG FAVNPDSIFD VQVKRLHAYK
RQLLNVLHIM YLYNRLKEDK GFAIYPQTFI FGAKASPTYH YAKKVIKLIH SVADKINHDP
DVRHSINVIF LENYRVSTAE RIFPASDVSE QISAASKEAS GTGNMKFMIN GALTIGTHDG
ANIEMLERVG TECIYTFGLK ADEVLDYAEK GGYLSREYYQ HDARIRQTAD QLINGFFEGE
AGEFEPIYDS LIAYNDEYFV LKDFASYIVA QERIQKDYLN KRLWAEKAVT NIAHAGYFSS
DRTIREYADD IWEIKPYQH
//
